|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
811-1477 |
0e+00 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 708.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 811 LALWGSGDRMWDWQLEDDRFFVTGPKQGSEAPAETNASRQMALVHPDDRPQVQAALESYLQGDTEFFEAEYRIKLTDANW 890
Cdd:COG5001 3 ALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 891 SWVLDRGKIVERDRSGKPLRLAGTFTDISMRRGQEEALRLSSQVLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIA 970
Cdd:COG5001 83 AALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 971 CKPFLFLTRGLYDRSFYQQIEHQLLNQKHWSGEVQIRTHCKQPLLVWMEVNQVLNSQGEASHFVVVFTD-----ITDRKQ 1045
Cdd:COG5001 163 ALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLaiarlITERKR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1046 AEEDLRLLANYDQLTGLPNRTLFQDRLDHALRQAHRNRNLVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAIRD 1125
Cdd:COG5001 243 AEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLRE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1126 GDTVARLGGDEFIIILEGLQKTEAATVIAEKLLAVFDRPFSLENFSLNVSPSIGISLYPDDAEDALELLKFADTAMYHAK 1205
Cdd:COG5001 323 GDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1206 SLGRNNFQFYTAKLNAYAVRHVQLEAGLKQALERDEFYLLYQPKFCVHSGKLTGMEALLRWESQELGPISPAEFIPLAEE 1285
Cdd:COG5001 403 AAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEE 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1286 TGQINAIGQWVLLSVCSQLERWQNQGLKAVPIAINLSAKQL-QSDIISSIEVALAMHGLAADLLEIELTESAVMQQPLES 1364
Cdd:COG5001 483 TGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLrDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEA 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1365 VEILNQLKGLGLSLAVDDFGTGYSSLAYLKRFPLDTLKIDREFVRDITKDPDDAAITSAIIVLAHSLELQVVAEGVETQA 1444
Cdd:COG5001 563 LETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEE 642
|
650 660 670
....*....|....*....|....*....|...
gi 917733955 1445 QLNFLAAQGCDQAQGFLLGRPMTEVQAQALLSR 1477
Cdd:COG5001 643 QLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
919-1477 |
4.64e-128 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 412.92 E-value: 4.64e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 919 SMRRGQEEALRLSSQVLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPF--LFLTR--GLYDRsfyQQIEHQL 994
Cdd:PRK10060 101 SVARDLSHGLSFAEQVVSEANSVIVILDSRGNIQRFNRLCEEYTGLKEHDVIGQSVfkLFMSRreAAASR---RNIRGFF 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 995 LNQKHWSGEVQIRThCKQPLLVWMEVNQVLNSQGEASHFVVVF-TDITDRKQAEEDLRLLANYDQLTGLPNRTLFQDRLD 1073
Cdd:PRK10060 178 RSGNAYEVERWIKT-RKGQRLFLFRNKFVHSGSGKNEIFLICSgTDITEERRAQERLRILANTDSITGLPNRNAIQELID 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1074 HALRQAHRNRnlVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAIRDGDTVARLGGDEFIIILEglQKTEAA-TV 1152
Cdd:PRK10060 257 HAINAADNNQ--VGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLAS--HTSQAAlEA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1153 IAEKLLAVFDRPFSLENFSLNVSPSIGISLYPDDAEDALELLKFADTAMYHAKSLGRNNFQFYTAKLNAYAVRHVQLEAG 1232
Cdd:PRK10060 333 MASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTN 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1233 LKQALERDEFYLLYQPKFCVhSGKLTGMEALLRWESQELGPISPAEFIPLAEETGQINAIGQWVLLSVCSQLERWQNQGL 1312
Cdd:PRK10060 413 LRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGI 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1313 KaVPIAINLSAKQLQSD-IISSIEVALAMHGLAADLLEIELTESAVMQQPLESVEILNQLKGLGLSLAVDDFGTGYSSLA 1391
Cdd:PRK10060 492 N-LRVAVNVSARQLADQtIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLS 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1392 YLKRFPLDTLKIDREFVRDITKDPDDAAITSAIIVLAHSLELQVVAEGVETQAQLNFLAAQGCDQAQGFLLGRPMTEVQA 1471
Cdd:PRK10060 571 QLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAF 650
|
....*.
gi 917733955 1472 QALLSR 1477
Cdd:PRK10060 651 ERWYKR 656
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
900-1475 |
6.56e-123 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 396.08 E-value: 6.56e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 900 VERDRSGKPLRLAGTFTDISMRRGQEEALRLSSQVLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFLFLTR 979
Cdd:COG2200 1 LLLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 980 GLYDRSFYQQIEHQLLNQKHWSGEVQIRTHCKQPLLVWMEVNQVLNSQGEASHFVVVFTDITDRKQAEEDLRLLANYDQL 1059
Cdd:COG2200 81 LLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1060 TGLPNRTLFQDRLDHALRQAHRNRNLVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAIRDGDTVARLGGDEFII 1139
Cdd:COG2200 161 LLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1140 ILEGLQKTEAATVIAEKLLAVFDRPFSLENFSLNVSPSIGISLYPDDAEDALELLKFADTAMYHAKSLGRNNFQFYTAkL 1219
Cdd:COG2200 241 LLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAA-A 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1220 NAYAVRHVQLEAGLKQALERDEFYLLYQPKFCVHSGKLTGMEALLRWESQELGPISPAEFIPLAEETGQINAIGQWVLLS 1299
Cdd:COG2200 320 EARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLER 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1300 VCSQLERWQNQGLKaVPIAINLSAKQL-QSDIISSIEVALAMHGLAADLLEIELTESAVMQQPLESVEILNQLKGLGLSL 1378
Cdd:COG2200 400 ALRQLARWPERGLD-LRLSVNLSARSLlDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1379 AVDDFGTGYSSLAYLKRFPLDTLKIDREFVRDITKDPDDAAITSAIIVLAHSLELQVVAEGVETQAQLNFLAAQGCDQAQ 1458
Cdd:COG2200 479 ALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQ 558
|
570
....*....|....*..
gi 917733955 1459 GFLLGRPMTEVQAQALL 1475
Cdd:COG2200 559 GYLFGRPLPLEELEALL 575
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
1233-1466 |
7.93e-108 |
|
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.
Pssm-ID: 238923 [Multi-domain] Cd Length: 240 Bit Score: 341.45 E-value: 7.93e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1233 LKQALERDEFYLLYQPKFCVHSGKLTGMEALLRWESQELGPISPAEFIPLAEETGQINAIGQWVLLSVCSQLERWQnQGL 1312
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQ-AGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1313 KAVPIAINLSAKQLQS-DIISSIEVALAMHGLAADLLEIELTESAVMQQPLESVEILNQLKGLGLSLAVDDFGTGYSSLA 1391
Cdd:cd01948 82 PDLRLSVNLSARQLRDpDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917733955 1392 YLKRFPLDTLKIDREFVRDITKDPDDAAITSAIIVLAHSLELQVVAEGVETQAQLNFLAAQGCDQAQGFLLGRPM 1466
Cdd:cd01948 162 YLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPL 236
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
1233-1468 |
1.40e-95 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 307.61 E-value: 1.40e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1233 LKQALERDEFYLLYQPKFCVHSGKLTGMEALLRWESQELGPISPAEFIPLAEETGQINAIGQWVLLSVCSQLERWQNQGL 1312
Cdd:smart00052 4 LRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1313 KAVPIAINLSAKQLQS-DIISSIEVALAMHGLAADLLEIELTESAVMQQPLESVEILNQLKGLGLSLAVDDFGTGYSSLA 1391
Cdd:smart00052 84 PPLLISINLSARQLISpDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917733955 1392 YLKRFPLDTLKIDREFVRDITKDPDDAAITSAIIVLAHSLELQVVAEGVETQAQLNFLAAQGCDQAQGFLLGRPMTE 1468
Cdd:smart00052 164 YLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
1026-1466 |
4.30e-94 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 322.87 E-value: 4.30e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1026 SQGEASHFVVVFTDIT--------DRKQAEEDLRLLANYDQLTGLPNRTLFQDRLDHALRQAHRnrnlVALLFLDLDRFK 1097
Cdd:PRK11359 340 SGAETSAFIERVADISqhlaalalEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAVS----PVVYLIGVDHFQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1098 HINDSLGHHVGDQLLKAVSSRLTQAIRDGDTVARLGGDEFIIILEGLQKTEAaTVIAEKLLAVFDRPFSLENFSLNVSPS 1177
Cdd:PRK11359 416 DVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNI-TQIADELRNVVSKPIMIDDKPFPLTLS 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1178 IGISLypDDAEDALELLKFADTAMYHAKSLGRNNFQFYTAKLNAYAVRHVQLEAGLKQALERDEFYLLYQPKFCVHSGKL 1257
Cdd:PRK11359 495 IGISY--DVGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGEL 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1258 TGMEALLRWESQELGPISPAEFIPLAEETGQINAIGQWVLLSVCSQLERWQNQGLKAVPIAINLSAKQLQS-DIISSIEV 1336
Cdd:PRK11359 573 YGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSnQLPNQVSD 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1337 ALAMHGLAADLLEIELTESAVMQQPLESVEILNQLKGLGLSLAVDDFGTGYSSLAYLKRFPLDTLKIDREFVRDITKDPD 1416
Cdd:PRK11359 653 AMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKR 732
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 917733955 1417 DAAITSAIIVLAHSLELQVVAEGVETQAQLNFLAAQGCDQAQGFLLGRPM 1466
Cdd:PRK11359 733 ILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPL 782
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
22-813 |
2.38e-90 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 315.39 E-value: 2.38e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 22 AEPVPQLKFQHVSSMNGLNQNSITSLYQDKAGILWIGTQDGLHSYNGIDFTLFQHDPYHSQTLSDNHVTDILQDGQGQLW 101
Cdd:COG3292 16 AQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGDPNSLPSNYIRALLEDSDGRLW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 102 VGTfNGGLNRLDLQTGVFTSIGRDQGLSSKKINRLALVGD-TLWIGSGNGLYALDTDSDELHELSLRQNISTDIQVLTpi 180
Cdd:COG3292 96 IGT-DGGLSRYDPKTDKFTRYPLDPGLPNNSIRSIAEDSDgNIWVGTSNGLYRYDPKTGKFKRFTLDGLPSNTITSLA-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 181 gkdalligsqsdgllllrneglkplplpdaehghpvqarQSEDGALWLaiddalwryppglnnpeliyrlpkpnrgilef 260
Cdd:COG3292 173 ---------------------------------------EDADGNLWV-------------------------------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 261 ifDNRGDIWLGGQQTGLIQLQLKEGQWQarHYRYDPsDPNSLSDNDVYSLLQDNNGILWIGSLFSGIDKVNLARQYFKHI 340
Cdd:COG3292 182 --DSDGNLWIGTDGNGLYRLDPNTGKFE--HITHDP-DPNSLSSNSIYSLFEDREGNLWVGTYGGGLNYLDPNNSKFKSY 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 341 YNNQQplERQRDNNIRAIFRAKDGLLY----LGTDRAGLFHITADGRFVSHHNqlakllgqDESFLDLTVSAIAQDSHQR 416
Cdd:COG3292 257 RHNDP--NGLSGNSVRSIAEDSDGNLWirlwIGTYGGGLFRLDPKTGKFKRYN--------PNGLPSNSVYSILEDSDGN 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 417 LWLASSGGlislnnsgemqlyrppgnkpairdllispdehiwlgvgnTLYHFNPETRGFQAHFVNEYLEDGpqeqMILSL 496
Cdd:COG3292 327 LWIGTSGG---------------------------------------GLYRYDPKTGKFTKFSEDNGLSNN----FIRSI 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 497 TTANNG-IWVGTTNGAYWLQPDTGQQQIIRGDR----LVNPMVRDILKDRDGNIWFATHG-GLSRLR--QGELQHFDRNQ 568
Cdd:COG3292 364 LEDSDGnLWVGTNGGLYRLDPKTGKFTNFTHDPdkngLSSNYINSIFEDSDGRLWIGTDGgGLYRYDpkTGKFKHFTTKD 443
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 569 GLPGNTVYAIEQDESGDFWFSSNSgisrfavdkekvltfneheglqalEFNGNVSWQDTDGSIWFGGINGLNHFYPQQVP 648
Cdd:COG3292 444 GLPSNTIYSILEDDNGNLWNFNSA------------------------SNLGLLSLLGGLLGGLNLGNAIKLPLSNLGLL 499
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 649 KVRKQPKLALAGYRMGNSYFPRLDLGHVPELTIPYSEQLVSFEISALDFAYPQRHRFSFFLEGWDKSWHPAQSLHEISYT 728
Cdd:COG3292 500 LTLLLLGINLSLVRSLISLLTLLLLALLLLLSLLLLLLLLLLLLLLLLLLLLLLLLLILLLLLLRLLLLLLLLELLERLL 579
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 729 NLAPGNYRLFVRHQLQHNPEGQEQLLLKLTVPAPFYRTTQAYLFYLTLTLILFSLWLRHFLAQRRLEQQTQSNIQLSEER 808
Cdd:COG3292 580 ALLLEIELLLTLLLLLLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLILLLLLLLLLLLLLLLLRLLLELLLLE 659
|
....*
gi 917733955 809 LKLAL 813
Cdd:COG3292 660 LELLL 664
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
786-1466 |
2.60e-84 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 300.82 E-value: 2.60e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 786 RHFLAQ----RRLEQQTQSNIQLSEeRLKLALWGSGDRMWDWQLE------DDRFFVTgpkqgSEAPAETNASRQM--AL 853
Cdd:PRK09776 386 LYFIAQiediNELKRTEQVNERLME-RITLANEAGGIGIWEWDLKpniiswDKRMFEL-----YEIPPHIKPTWQVwyAC 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 854 VHPDDRPQVQAALESYLQGDTEFfEAEYRIKLTDANwSWVLDRGKIVeRDRSGKPLRLAGTFTDISMRRGQEEAL----- 928
Cdd:PRK09776 460 LHPEDRQRVEKEIRDALQGRSPF-KLEFRIVVKDGV-RHIRALANRV-LNKDGEVERLLGINMDMTEVRQLNEALfqeke 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 929 RLssQV-LESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFLFLTRGLYDRS--FYQQIEHQLLNQKHWSGEVQ 1005
Cdd:PRK09776 537 RL--HItLDSIGEAVVCTDMAMKVTFMNPVAEKMTGWTQEEALGVPLLTVLHITFGDNgpLMENIYSCLTSRSAAYLEQD 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1006 IRTHCK--QPLLVWMEVNQVLNSQGEASHFVVVFTDITDRKQAEEDLRLLANYDQLTGLPNRTLFQDRLDHALRQAHRNR 1083
Cdd:PRK09776 615 VVLHCRsgGSYDVHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTH 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1084 NLVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAIRDGDTVARLGGDEFIIILEGLQkTEAATVIAEKLL-AVFD 1162
Cdd:PRK09776 695 QRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCN-VESARFIATRIIsAIND 773
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1163 RPFSLENFSLNVSPSIGISLYPDDAEDALELLKFADTAMYHAKSLGRNNFQFYTA-KLNAYAVRH-VQLEAGLKQALERD 1240
Cdd:PRK09776 774 YHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYEPqQAAAHSEHRaLSLAEQWRMIKENQ 853
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1241 EFYLLYQ------PKFCVHsgkltgMEALLR-WESQelGP-ISPAEFIPLAEETGQINAIGQWvllsVCSQLERWQNQGL 1312
Cdd:PRK09776 854 LMMLAHGvaspriPEARNH------WLISLRlWDPE--GEiIDEGAFRPAAEDPALMHALDRR----VIHEFFRQAAKAV 921
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1313 --KAVPIAINLSAKQLQS-DIISSIEVALAMHGLAADLLEIELTESAVMQQPLESVEILNQLKGLGLSLAVDDFGTGYSS 1389
Cdd:PRK09776 922 asKGLSIALPLSVAGLSSpTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSS 1001
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917733955 1390 LAYLKRFPLDTLKIDREFVRDITKDPDDAAITSAIIVLAHSLELQVVAEGVETQAQLNFLAAQGCDQAQGFLLGRPM 1466
Cdd:PRK09776 1002 FNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQ 1078
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
1044-1467 |
1.70e-78 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 273.90 E-value: 1.70e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1044 KQAEEDLRLLANYDQLTGLPNRTLFQDRLDHALRQAHRnrnlVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAI 1123
Cdd:PRK13561 221 QRQYEEQSRNATRFPVSDLPNKALLMALLEQVVARKQT----TALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1124 RDGDTVARLGGDEFIIILEGLQKTEAATVIAEKLLAVFDRPFSLENFSLNVSPSIGISLYPDDaEDALELLKFADTAMYH 1203
Cdd:PRK13561 297 SPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGD-LTAEQLYSRAISAAFT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1204 AKSLGRNNFQFYTAKLNAYAVRHVQLEAGLKQALERDEFYLLYQPKFCVHSGKLTGMEALLRWE----SQELgpisPAEF 1279
Cdd:PRK13561 376 ARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQqpdgSWDL----PEGL 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1280 IPLAEETGQINAIGQWVLLSVCSQLERWQNQGLkAVPIAINLSAKQL-QSDIISSIEVALAMHGLAADLLEIELTESAVM 1358
Cdd:PRK13561 452 IDRIESCGLMVTVGHWVLEESCRLLAAWQERGI-MLPLSVNLSALQLmHPNMVADMLELLTRYRIQPGTLILEVTESRRI 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1359 QQPLESVEILNQLKGLGLSLAVDDFGTGYSSLAYLKRF---PLDTLKIDREFVRDItkdPDDAAITSAIIVLAHSLELQV 1435
Cdd:PRK13561 531 DDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFVDGL---PEDDSMVAAIIMLAQSLNLQV 607
|
410 420 430
....*....|....*....|....*....|..
gi 917733955 1436 VAEGVETQAQLNFLAAQGCDQAQGFLLGRPMT 1467
Cdd:PRK13561 608 IAEGVETEAQRDWLLKAGVGIAQGFLFARALP 639
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
1233-1465 |
1.48e-75 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 250.70 E-value: 1.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1233 LKQALERDEFYLLYQPKFCVHSGKLTGMEALLRWESQELGPISPAEFIPLAEETGQINAIGQWVLLSVCSQLERWQNQGL 1312
Cdd:pfam00563 4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1313 kaVPIAINLSAKQL-QSDIISSIEVALAMHGLAADLLEIELTESAVMQQPLESVEILNQLKGLGLSLAVDDFGTGYSSLA 1391
Cdd:pfam00563 84 --IKLSINLSPASLaDPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917733955 1392 YLKRFPLDTLKIDREFVRDITKDPDDAAITSAIIVLAHSLELQVVAEGVETQAQLNFLAAQGCDQAQGFLLGRP 1465
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
1051-1473 |
2.77e-73 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 258.72 E-value: 2.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1051 RLLANYDQlTGLPNRTLFQDRLDHALRQAHRnRNLVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAIRDGDTVA 1130
Cdd:PRK11829 230 RISHRFPV-TELPNRSLFISLLEKEIASSTR-TDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1131 RLGGDEFIIILEGLQKTEAATVIAEKLLAVFDRPFSLENFSLNVSPSIGISLYPDDAEDALELLKFADTAMYHAKSLGRN 1210
Cdd:PRK11829 308 QLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRN 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1211 NFQFYTAKLNAYAVRHVQLEAGLKQALERDEFYLLYQPKFCVHSGKLTGMEALLRWESQELGPISPAEFIPLAEETGQIN 1290
Cdd:PRK11829 388 QIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMV 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1291 AIGQWVLLSVCSQLERWQNQGLkAVPIAINLSAKQLQ-SDIISSIEVALAMHGLAADLLEIELTESAVMQQPLESVEILN 1369
Cdd:PRK11829 468 PLGNWVLEEACRILADWKARGV-SLPLSVNISGLQVQnKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLR 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1370 QLKGLGLSLAVDDFGTGYSSLAYL---KRFPLDTLKIDREFVRDItkdPDDAAITSAIIVLAHSLELQVVAEGVETQAQL 1446
Cdd:PRK11829 547 ELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQR 623
|
410 420
....*....|....*....|....*..
gi 917733955 1447 NFLAAQGCDQAQGFLLGRPMTEVQAQA 1473
Cdd:PRK11829 624 QWLLEHGIQCGQGFLFSPPLPRAEFEA 650
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
1229-1466 |
1.21e-72 |
|
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];
Pssm-ID: 443970 [Multi-domain] Cd Length: 528 Bit Score: 252.91 E-value: 1.21e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1229 LEAGLKQALERDEFYLLYQPKFCVHSGKLTGMEALLRWESQELGPISPAEFIPLAEETGQINAIGQWVLLSVCSQLERW- 1307
Cdd:COG4943 272 PRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLl 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1308 -QNQGLKavpIAINLSAKQLQS-DIISSIEVALAMHGLAADLLEIELTESAVMQQPlESVEILNQLKGLGLSLAVDDFGT 1385
Cdd:COG4943 352 aADPDFH---ISINLSASDLLSpRFLDDLERLLARTGVAPQQIVLEITERGFIDPA-KARAVIAALREAGHRIAIDDFGT 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1386 GYSSLAYLKRFPLDTLKIDREFVRDITKDPDDAAITSAIIVLAHSLELQVVAEGVETQAQLNFLAAQGCDQAQGFLLGRP 1465
Cdd:COG4943 428 GYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKP 507
|
.
gi 917733955 1466 M 1466
Cdd:COG4943 508 L 508
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
1014-1215 |
1.52e-68 |
|
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];
Pssm-ID: 441801 [Multi-domain] Cd Length: 275 Bit Score: 232.18 E-value: 1.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1014 LLVWMEVNQVLNSQGEASHFVVVFTDITDRKQAEEDLRLLANYDQLTGLPNRTLFQDRLDHALRQAHRNRNLVALLFLDL 1093
Cdd:COG2199 74 LLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1094 DRFKHINDSLGHHVGDQLLKAVSSRLTQAIRDGDTVARLGGDEFIIILEGLqKTEAATVIAEKLLAVFDR-PFSLENFSL 1172
Cdd:COG2199 154 DHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGT-DLEEAEALAERLREALEQlPFELEGKEL 232
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 917733955 1173 NVSPSIGISLYPDDAEDALELLKFADTAMYHAKSLGRNNFQFY 1215
Cdd:COG2199 233 RVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
1055-1213 |
5.31e-66 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 220.12 E-value: 5.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1055 NYDQLTGLPNRTLFQDRLDHALRQAHRNRNLVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAIRDGDTVARLGG 1134
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 917733955 1135 DEFIIILEGLQKTEAATvIAEKLLAVFDRPFSLENFSLNVSPSIGISLYPDDAEDALELLKFADTAMYHAKSLGRNNFQ 1213
Cdd:cd01949 81 DEFAILLPGTDLEEAEA-LAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
1054-1211 |
8.78e-62 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 207.88 E-value: 8.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1054 ANYDQLTGLPNRTLFQDRLDHALRQAHRNRNLVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAIRDGDTVARLG 1133
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1134 GDEFIIILEGLQKTEA--ATVIAEKLLAVFDRPFSLENFSLNVSPSIGISLYPDDAEDALELLKFADTAMYHAKSLGRNN 1211
Cdd:pfam00990 81 GDEFAILLPETSLEGAqeLAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
1052-1215 |
1.96e-59 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 201.32 E-value: 1.96e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1052 LLANYDQLTGLPNRTLFQDRLDHALRQAHRNRNLVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAIRDGDTVAR 1131
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1132 LGGDEFIIILEGLQkTEAATVIAEKLLAVFDRPFSLENFSLNVSPSIGISLYPDDAEDALELLKFADTAMYHAKSLGRNN 1211
Cdd:smart00267 81 LGGDEFALLLPETS-LEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 917733955 1212 FQFY 1215
Cdd:smart00267 160 VAVY 163
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
1235-1467 |
2.64e-44 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 169.40 E-value: 2.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1235 QALERDEFYLLYQPKFCVHSGKLTGMEALLRWESQELGPISPAEFIPLAEETGQINAIGQWVLLSVCSQLERWQNQGLKA 1314
Cdd:PRK10551 270 TGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVLPVG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1315 VPIAINLSAKQLQSD-IISSIEVALAMhgLAADLLEI--ELTESAVMQQpLESVEILNQLKGLGLSLAVDDFGTGYSSLA 1391
Cdd:PRK10551 350 AKLGINISPAHLHSDsFKADVQRLLAS--LPADHFQIvlEITERDMVQE-EEATKLFAWLHSQGIEIAIDDFGTGHSALI 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917733955 1392 YLKRFPLDTLKIDREFVRDITKDPDDAAITSAIIVLAHSLELQVVAEGVETQAQLNFLAAQGCDQAQGFLLGRPMT 1467
Cdd:PRK10551 427 YLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLP 502
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
1053-1210 |
2.16e-41 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 149.79 E-value: 2.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1053 LANYDQLTGLPNRTLFQDRLDHALRQAHRNRNLVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAIRDGDTVARL 1132
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1133 GGDEFIIILEGLQKTEAATvIAEKL-LAVFDRPFSLENFS-LNVSPSIGISLYPDDAEDALELLKFADTAMYHAKSLGRN 1210
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALS-KAERLrDAINSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
1043-1210 |
3.80e-35 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 140.81 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1043 RKQAEEDLRL-------LANYDQLTGLPNRTLFQDRLDHALRQAH-RNRNLvALLFLDLDRFKHINDSLGHHVGDQLLKA 1114
Cdd:PRK09581 274 RKRYQDALRNnleqsieMAVTDGLTGLHNRRYFDMHLKNLIERANeRGKPL-SLMMIDIDHFKKVNDTYGHDAGDEVLRE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1115 VSSRLTQAIRDGDTVARLGGDEFIIILEGLQkTEAATVIAEKL-LAVFDRPFSLEN--FSLNVSPSIGISLYPDDAEDAL 1191
Cdd:PRK09581 353 FAKRLRNNIRGTDLIARYGGEEFVVVMPDTD-IEDAIAVAERIrRKIAEEPFIISDgkERLNVTVSIGVAELRPSGDTIE 431
|
170
....*....|....*....
gi 917733955 1192 ELLKFADTAMYHAKSLGRN 1210
Cdd:PRK09581 432 ALIKRADKALYEAKNTGRN 450
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
1050-1210 |
2.93e-31 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 125.18 E-value: 2.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1050 LRLLANYDQLTGLPNRTLFQDRLDHALRQAHRnRNLvALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAIRDGDTV 1129
Cdd:PRK09894 125 LTIRSNMDVLTGLPGRRVLDESFDHQLRNREP-QNL-YLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1130 ARLGGDEFIIILEGLQKTEAATVIAEKLLAVFDRPFSLENFSLNVSPSIGIS-LYPDDAEDalELLKFADTAMYHAKSLG 1208
Cdd:PRK09894 203 YRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSrAFPEETLD--VVIGRADRAMYEGKQTG 280
|
..
gi 917733955 1209 RN 1210
Cdd:PRK09894 281 RN 282
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
921-1141 |
2.34e-29 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 118.59 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 921 RRGQEEALRLSSQVLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFLFLTRGLYDRSFYQQIEHQLLNQKHW 1000
Cdd:COG2202 3 EEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1001 SGEVQIRTHCKQPLLVWMEVNQVLNSQGEASHFVVVFTDITDRKQAEEDLRLLANYDQLTGLPNRTLFQdRLDHALRQAH 1080
Cdd:COG2202 83 RGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIF-VLDLDGRILY 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917733955 1081 RNRNLVALLFLDLDRF--KHINDSLGHHVGDQLLKAVSSRLTQAIRDGDTVARLGGDEFIIIL 1141
Cdd:COG2202 162 VNPAAEELLGYSPEELlgKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVW 224
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
1048-1210 |
3.10e-27 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 118.58 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1048 EDLRLLANYDQLTGLPNRTLFQDRLDHALRQAHRNRNLVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAIRDGD 1127
Cdd:PRK15426 392 SSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQD 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1128 TVARLGGDEFIIILEGLQKTEAATViAEKL-LAVFDRP-FSLENFSLNVSPSIGISLYPDDAEDALE-LLKFADTAMYHA 1204
Cdd:PRK15426 472 VAGRVGGEEFCVVLPGASLAEAAQV-AERIrLRINEKEiLVAKSTTIRISASLGVSSAEEDGDYDFEqLQSLADRRLYLA 550
|
....*.
gi 917733955 1205 KSLGRN 1210
Cdd:PRK15426 551 KQAGRN 556
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
853-1050 |
8.01e-27 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 111.27 E-value: 8.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 853 LVHPDDRPQVQAALESYLQGDtEFFEAEYRIKLTDANWSWVLDRGKIVeRDRSGKPLRLAGTFTDISMRRGQEEALRLSS 932
Cdd:COG2202 59 LLPPEDDDEFLELLRAALAGG-GVWRGELRNRRKDGSLFWVELSISPV-RDEDGEITGFVGIARDITERKRAEEALRESE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 933 Q----VLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFLFLTRGLYDRSFYQQIEhQLLNQKHWSGEVQIRT 1008
Cdd:COG2202 137 ErlrlLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLR-RLLEGGRESYELELRL 215
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 917733955 1009 HCKQPLLVWMEVNQV-LNSQGEASHFVVVFTDITDRKQAEEDL 1050
Cdd:COG2202 216 KDGDGRWVWVEASAVpLRDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
1029-1205 |
1.38e-22 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 102.39 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1029 EASHFVVVFTDITDRKQaEEDLRLLAN---------YDQLTGLPNRTLFQDRLDhALRQAHRNRNLVALLFLDLDRFKHI 1099
Cdd:PRK09966 215 EFHRFALDFNSLLDEME-EWQLRLQAKnaqllrtalHDPLTGLANRAAFRSGIN-TLMNNSDARKTSALLFLDGDNFKYI 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1100 NDSLGHHVGDQLLKAVSSRLTQAIRDGDTVARLGGDEFIIILEGLQKTEAATVIAEKLLAVFDRPFSLENFSL-NVSPSI 1178
Cdd:PRK09966 293 NDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQtTMTLSI 372
|
170 180
....*....|....*....|....*..
gi 917733955 1179 GISLYPDDAEdALELLKFADTAMYHAK 1205
Cdd:PRK09966 373 GYAMTIEHAS-AEKLQELADHNMYQAK 398
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
1050-1210 |
5.19e-22 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 99.90 E-value: 5.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1050 LRLLANYDQLTGLPNR----TLFQDRLDHALRQaHRNrnlVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAIRD 1125
Cdd:PRK10245 201 LQVMSTRDGMTGVYNRrhweTLLRNEFDNCRRH-HRD---ATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRG 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1126 GDTVARLGGDEFIIILEGlqkTEAATVIAeKLLAVFDRpfsLENFSLNVSP------SIGISLYPDDAEDALELLKFADT 1199
Cdd:PRK10245 277 SDVIGRFGGDEFAVIMSG---TPAESAIT-AMSRVHEG---LNTLRLPNAPqvtlriSVGVAPLNPQMSHYREWLKSADL 349
|
170
....*....|.
gi 917733955 1200 AMYHAKSLGRN 1210
Cdd:PRK10245 350 ALYKAKNAGRN 360
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
1057-1459 |
3.12e-17 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 87.23 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1057 DQLTGLPNRTLFQDRLDHALRQAHRNRNLVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAI-RDGDTV-ARLGG 1134
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVmRYPGALlARYSR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1135 DEFIIILEGLQKTEAATvIAEKLLAVFDrpfslenfSLNVSPS--------IGISLYpDDAEDALELLKFADTAMYHAKS 1206
Cdd:PRK11059 311 SDFAVLLPHRSLKEADS-LASQLLKAVD--------ALPPPKMldrddflhIGICAY-RSGQSTEQVMEEAEMALRSAQL 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1207 LGRNNFQFYTaklnayavRHVQLEAG---------LKQALERDEFYLLYQPKFCVHsGKLTGMEALLRW--ESQELgpIS 1275
Cdd:PRK11059 381 QGGNGWFVYD--------KAQLPEKGrgsvrwrtlLEQTLVRGGPRLYQQPAVTRD-GKVHHRELFCRIrdGQGEL--LS 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1276 PAEFIPLAEETGQINAIGQWVLLSVCSQLERWQNQglkavPIAINLSAKQLQSdiissievALAMHGLAADLLE------ 1349
Cdd:PRK11059 450 AELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEE-----NLSINLSVDSLLS--------RAFQRWLRDTLLQcprsqr 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1350 ----IELTESAVMQQPLESVEILNQLKGLGLSLAVDDFGTGYSSLAYLKRFPLDTLKIDREFVRDITKDPDDA-AITSAI 1424
Cdd:PRK11059 517 krliFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQlFVRSLV 596
|
410 420 430
....*....|....*....|....*....|....*
gi 917733955 1425 IVLAHSlELQVVAEGVETQAQLNFLAAQGCDQAQG 1459
Cdd:PRK11059 597 GACAGT-ETQVFATGVESREEWQTLQELGVSGGQG 630
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
1057-1205 |
9.39e-16 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 81.93 E-value: 9.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1057 DQLTGLPNRTLFQDRLDHALRQAHRNRNLVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAIRDGDTVARLGGDE 1136
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDE 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 917733955 1137 FIIILEGLQKTEAATVIA--EKLLAVFDrPFSLENFSlnvspSIGISLYPDDA-EDAlelLKFADTAMYHAK 1205
Cdd:NF040885 424 FCIILIDYEEAEAQNLIEriRQHLRTID-PDKRVSFS-----WGAYQMQPGDTlDDA---YKAADERLYLNK 486
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
853-1051 |
2.84e-15 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 80.40 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 853 LVHPDDrPQVQAALESYLQGDTEFFEAEYRIKLTDANWSWVLDRGKIVErDRSGKPLRLAGTFTDISMRRGQEEALRLSS 932
Cdd:COG5809 63 FLHPDD-EKELREILKLLKEGESRDELEFELRHKNGKRLEFSSKLSPIF-DQNGDIEGMLAISRDITERKRMEEALRESE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 933 Q----VLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFLFLTRGLYDRSFYQQIEHQLLNQKHWSGEVQIRT 1008
Cdd:COG5809 141 EkfrlIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWT 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 917733955 1009 HCKQplLVWMEVNQV-LNSQGEASHFVVVFTDITDRKQAEEDLR 1051
Cdd:COG5809 221 KDGR--WRLLEASGApIKKNGEVDGIVIIFRDITERKKLEELLR 262
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
924-1050 |
3.50e-14 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 70.40 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 924 QEEALRlssQVLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFLFLTRGLYDRSFYQQIEHQLLNQKHW-SG 1002
Cdd:TIGR00229 1 SEERYR---AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPvSE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 917733955 1003 EVQIRThcKQPLLVWMEVN-QVLNSQGEASHFVVVFTDITDRKQAEEDL 1050
Cdd:TIGR00229 78 ERRVRR--KDGSEIWVEVSvSPIRTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
925-1054 |
6.27e-14 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 75.27 E-value: 6.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 925 EEALRLSSQVLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPF--LFLTRGLYDRSFYQQIEHqllNQKHWSG 1002
Cdd:COG3852 3 RESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLaeLFPEDSPLRELLERALAE---GQPVTER 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 917733955 1003 EVQIRTHCKQPLLVWMEVNQVLNSQGEaSHFVVVFTDITDRKQAEEDLRLLA 1054
Cdd:COG3852 80 EVTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAE 130
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
851-914 |
3.07e-13 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 66.59 E-value: 3.07e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917733955 851 MALVHPDDRPQVQAALESYLQGDtEFFEAEYRIKLTDANWSWVLDRGKIVeRDRSGKPLRLAGT 914
Cdd:pfam08447 27 LDLVHPDDRERVREALWEALKGG-EPYSGEYRIRRKDGEYRWVEARARPI-RDENGKPVRVIGV 88
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
356-602 |
7.40e-13 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 70.43 E-value: 7.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 356 RAIFRAKDGLLYL---GTDRAGLFHiTADGRFVSHhnQLAKLLGqdesfldltVSAIAQDSHQRLWLASSGG--LISLN- 429
Cdd:COG4257 20 RDVAVDPDGAVWFtdqGGGRIGRLD-PATGEFTEY--PLGGGSG---------PHGIAVDPDGNLWFTDNGNnrIGRIDp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 430 NSGEMQLYRPPGNKPAIRDLLISPDEHIW--LGVGNTLYHFNPETRGFQAHfvneyleDGPQEQMILS-LTTANNG-IWV 505
Cdd:COG4257 88 KTGEITTFALPGGGSNPHGIAFDPDGNLWftDQGGNRIGRLDPATGEVTEF-------PLPTGGAGPYgIAVDPDGnLWV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 506 gTTNGA---YWLQPDTGQQQIIRGDR-LVNPmvRDILKDRDGNIWFATHGGlsrlrqGELQHFDRNQG------LPGNTV 575
Cdd:COG4257 161 -TDFGAnaiGRIDPDTGTLTEYALPTpGAGP--RGLAVDPDGNLWVADTGS------GRIGRFDPKTGtvteypLPGGGA 231
|
250 260 270
....*....|....*....|....*....|.
gi 917733955 576 --YAIEQDESGDFWFSSNSG--ISRFAVDKE 602
Cdd:COG4257 232 rpYGVAVDGDGRVWFAESGAnrIVRFDPDTE 262
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
914-1059 |
3.62e-12 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 70.53 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 914 TFTDISMRRGQEEALRLSSQVL----ESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFLFLTRGLYDRSFYQQ 989
Cdd:COG5805 138 ALRDITKKKKIEEILQEQEERLqtliENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKER 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917733955 990 IEHqllNQKHWS-GEVQIRTHCKQPLLVWMEVN--QVLNSQGEASHFVVVFTDITDRKQAEEdlrLLANYDQL 1059
Cdd:COG5805 218 IES---ITEVWQeFIIEREIITKDGRIRYFEAVivPLIDTDGSVKGILVILRDITEKKEAEE---LMARSEKL 284
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
925-1142 |
7.06e-12 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 69.62 E-value: 7.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 925 EEALRLSSQ----VLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFLFLTRGLYDRSFYQQIehQLLNQKHW 1000
Cdd:COG5809 7 ELQLRKSEQrfrsLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREIL--KLLKEGES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1001 SGEVQIRTHCKQPLLVWME--VNQVLNSQGEASHFVVVFTDITDRKQAEEDL-------RLLANYdqltgLPNRTLFQDr 1071
Cdd:COG5809 85 RDELEFELRHKNGKRLEFSskLSPIFDQNGDIEGMLAISRDITERKRMEEALreseekfRLIFNH-----SPDGIIVTD- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917733955 1072 LDHALRQAhrnrNLVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAIRDGD----TVARLGGDEFIIILE 1142
Cdd:COG5809 159 LDGRIIYA----NPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGiaqgEVRFWTKDGRWRLLE 229
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
1109-1205 |
4.42e-10 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 60.31 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1109 DQLLKAVSSR-LTQAIrdgDTVARLGGDEFIIILEGLQKtEAATVIAEKLLAVFDRPfslenFSLNVSPSIGISlypdda 1187
Cdd:COG3706 100 DYLTKPFDPEeLLARV---DLVARYGGEEFAILLPGTDL-EGALAVAERIREAVAEL-----PSLRVTVSIGVA------ 164
|
90
....*....|....*...
gi 917733955 1188 edALELLKFADtAMYHAK 1205
Cdd:COG3706 165 --GDSLLKRAD-ALYQAR 179
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
1319-1474 |
9.48e-10 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 62.51 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1319 INLSAKQLQSDIISSievalamhgLAADLLEIELTESAVMQQPLesVEILNQLKGLGLSLAVDDFGTGYSSLAYLKRFpl 1398
Cdd:COG3434 66 INFTEELLLSDLPEL---------LPPERVVLEILEDVEPDEEL--LEALKELKEKGYRIALDDFVLDPEWDPLLPLA-- 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917733955 1399 DTLKIDrefVRDItkDPDDAAitsAIIVLAHSLELQVVAEGVETQAQLNFLAAQGCDQAQGFLLGRPMTeVQAQAL 1474
Cdd:COG3434 133 DIIKID---VLAL--DLEELA---ELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEI-LKGKKL 199
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
1085-1181 |
1.45e-09 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 57.75 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1085 LVALLFLDLDRFKHINDSLGHHVGDQLLKAVSSRLTQAI-RDGDTVARLGGDEFIIILeGLQKTEAATVIAEKLLAVFDR 1163
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVS-GLDHPAAAVAFAEDMREAVSA 79
|
90
....*....|....*....
gi 917733955 1164 -PFSLENfslNVSPSIGIS 1181
Cdd:cd07556 80 lNQSEGN---PVRVRIGIH 95
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
790-928 |
1.57e-09 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 60.42 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 790 AQRRLEQQtqsnIQLSEERLKLALWGSGDRMWDWQLEDDRFFV--TGPKQGSEAPAETNASRQMALVHPDDRPQVQAALE 867
Cdd:COG2202 124 ERKRAEEA----LRESEERLRLLVENAPDGIFVLDLDGRILYVnpAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLR 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917733955 868 SYLQGDTEFFEAEYRIKLTDANWSWVldRGKIVERDRSGKPLRLAGTFTDISMRRGQEEAL 928
Cdd:COG2202 200 RLLEGGRESYELELRLKDGDGRWVWV--EASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
938-1040 |
1.58e-09 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 56.49 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 938 MNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFLFLTRGLYDRSFYQQIEHQLLNQKHWSGEVQIRTHCKQPLLVW 1017
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 917733955 1018 MEVNQVLNSQGEASHFVVVFTDI 1040
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| Y_Y_Y |
pfam07495 |
Y_Y_Y domain; This domain is mostly found at the end of the beta propellers (pfam07494) in a ... |
696-759 |
2.43e-09 |
|
Y_Y_Y domain; This domain is mostly found at the end of the beta propellers (pfam07494) in a family of two component regulators. However they are also found tandemly repeated in Swiss:Q891H4 without other signal conduction domains being present. It's named after the conserved tyrosines found in the alignment. The exact function is not known.
Pssm-ID: 400051 [Multi-domain] Cd Length: 65 Bit Score: 54.67 E-value: 2.43e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917733955 696 DFAYPQRHRFSFFLEGWDKSWHPAQSLHEISYTNLAPGNYRLFVRHQLQHNPEGQEQLLLKLTV 759
Cdd:pfam07495 1 NYDGPENLLYRYRLEGFDGEWVELGDYSEASYTNLPPGKYTLKVKAKDNDGNWSYDDASLNFTI 64
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
932-1040 |
6.03e-09 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 55.12 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 932 SQVLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFLFLTRGLYDRSFYQQIEHQLLNQKHW-SGEVQIRTHC 1010
Cdd:pfam00989 4 RAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESrGFEVSFRVPD 83
|
90 100 110
....*....|....*....|....*....|
gi 917733955 1011 KQPLLVWMEVNQVLNSQGEASHFVVVFTDI 1040
Cdd:pfam00989 84 GRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
948-1042 |
8.53e-09 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 54.00 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 948 NYRIISVNPAFCSTTGFSEQQIACKPFLFLTRGLYDRSFYQQIEHQLlnQKHWSGEVQIRTHCKQPLLVWMEVNQVLNSQ 1027
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREG--KAVREFEVVLYRKDGEPFPVLVSLAPIRDDG 78
|
90
....*....|....*
gi 917733955 1028 GEASHFVVVFTDITD 1042
Cdd:pfam13426 79 GELVGIIAILRDITE 93
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
910-1048 |
1.64e-08 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 58.82 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 910 RLAGTFTDI-----SMRRGQEEALRLSSQVLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFLFLTRGLydr 984
Cdd:COG5000 66 ELARAFNRMtdqlkEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPEL--- 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 917733955 985 SFYQQIEHQLlnQKHWSGEVQIRTHCKQPLLVWMEvnqVLNSQGeashFVVVFTDITDRKQAEE 1048
Cdd:COG5000 143 DLAELLREAL--ERGWQEEIELTRDGRRTLLVRAS---PLRDDG----YVIVFDDITELLRAER 197
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
85-321 |
2.00e-08 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 57.34 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 85 SDNHVTDILQDGQGQLWV-GTFNGGLNRLDLQTGVFTSIGRDQGLSSKKInrlALVGD-TLWIG--SGNGLYALDTDSDE 160
Cdd:COG4257 15 PGSGPRDVAVDPDGAVWFtDQGGGRIGRLDPATGEFTEYPLGGGSGPHGI---AVDPDgNLWFTdnGNNRIGRIDPKTGE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 161 LHELSLRQNIS--TDIQVLtpiGKDALLIGSQSDGLLL---LRNEGLKPLPLPdAEHGHPVQARQSEDGALWLA--IDDA 233
Cdd:COG4257 92 ITTFALPGGGSnpHGIAFD---PDGNLWFTDQGGNRIGrldPATGEVTEFPLP-TGGAGPYGIAVDPDGNLWVTdfGANA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 234 LWRYPPGLNNPElIYRLPKPNRGILEFIFDNRGDIWLGGQQTGLIqlqlkegqwqarhYRYDPSD------PNSLSDNDV 307
Cdd:COG4257 168 IGRIDPDTGTLT-EYALPTPGAGPRGLAVDPDGNLWVADTGSGRI-------------GRFDPKTgtvteyPLPGGGARP 233
|
250
....*....|....
gi 917733955 308 YSLLQDNNGILWIG 321
Cdd:COG4257 234 YGVAVDGDGRVWFA 247
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
408-645 |
3.48e-08 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 56.57 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 408 AIAQDSHQRLWLASSGG--LISLN-NSGEMQLYRPPGNkPAIRDLLISPDEHIWLG--VGNTLYHFNPETRGFQAHfvne 482
Cdd:COG4257 21 DVAVDPDGAVWFTDQGGgrIGRLDpATGEFTEYPLGGG-SGPHGIAVDPDGNLWFTdnGNNRIGRIDPKTGEITTF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 483 yleDGPQEQMIL-SLTTANNG-IWV--GTTNGAYWLQPDTGQQQIIRGDRlVNPMVRDILKDRDGNIWFATHGGlSRLRQ 558
Cdd:COG4257 96 ---ALPGGGSNPhGIAFDPDGnLWFtdQGGNRIGRLDPATGEVTEFPLPT-GGAGPYGIAVDPDGNLWVTDFGA-NAIGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 559 -----GELQHFDRNQglPGNTVYAIEQDESGDFWF--SSNSGISRFAVDKEKVLTFNEHEGLQ---ALEFngnvswqDTD 628
Cdd:COG4257 171 idpdtGTLTEYALPT--PGAGPRGLAVDPDGNLWVadTGSGRIGRFDPKTGTVTEYPLPGGGArpyGVAV-------DGD 241
|
250
....*....|....*....
gi 917733955 629 GSIWFG--GINGLNHFYPQ 645
Cdd:COG4257 242 GRVWFAesGANRIVRFDPD 260
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
852-931 |
4.02e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 58.15 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 852 ALVHPDDRPQVQAALESYLQGDTEFFEAEYRIKLTDANWSWVLDRGKiVERDRSGKPLRLAGTFTDISMRRGQEEALRLS 931
Cdd:PRK13560 523 AIIHPADLEQVAAEVAEFAAQGVDRFEQEYRILGKGGAVCWIDDQSA-AERDEEGQISHFEGIVIDISERKHAEEKIKAA 601
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
447-638 |
9.15e-08 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 55.03 E-value: 9.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 447 RDLLISPDEHIW--LGVGNTLYHFNPETRGFQAHFVNEYledgpqeQMILSLTTANNG-IWV-GTTNGAYW-LQPDTGQQ 521
Cdd:COG4257 20 RDVAVDPDGAVWftDQGGGRIGRLDPATGEFTEYPLGGG-------SGPHGIAVDPDGnLWFtDNGNNRIGrIDPKTGEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 522 QIIRG-DRLVNPMvrDILKDRDGNIWFATHGGlsrlrqGELQHFDRNQG--------LPGNTVYAIEQDESGDFWFSSNS 592
Cdd:COG4257 93 TTFALpGGGSNPH--GIAFDPDGNLWFTDQGG------NRIGRLDPATGevtefplpTGGAGPYGIAVDPDGNLWVTDFG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 917733955 593 G--ISRFAVDKEKVLTFNEHEGLQAleFNGnVSWqDTDGSIWFGGING 638
Cdd:COG4257 165 AnaIGRIDPDTGTLTEYALPTPGAG--PRG-LAV-DPDGNLWVADTGS 208
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
248-510 |
2.38e-07 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 53.87 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 248 YRLPKPNRGILEFIFDNRGDIWLGGQQTGLI-QLQLKEGQWQarhyRYDPSDPNSlsdndVYSLLQDNNGILWIGSLFSG 326
Cdd:COG4257 10 YPVPAPGSGPRDVAVDPDGAVWFTDQGGGRIgRLDPATGEFT----EYPLGGGSG-----PHGIAVDPDGNLWFTDNGNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 327 ----IDKVNLARQYFKHiynnqqPLERQRDNNIRAifrAKDGLLY---LGTDRAGLFhITADGRFVSHHnqlaklLGQDE 399
Cdd:COG4257 81 rigrIDPKTGEITTFAL------PGGGSNPHGIAF---DPDGNLWftdQGGNRIGRL-DPATGEVTEFP------LPTGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 400 SFLdltvSAIAQDSHQRLWLASSGG--LISLNN-SGEMQLYRPPGNKPAIRDLLISPDEHIWLG--VGNTLYHFNPETRG 474
Cdd:COG4257 145 AGP----YGIAVDPDGNLWVTDFGAnaIGRIDPdTGTLTEYALPTPGAGPRGLAVDPDGNLWVAdtGSGRIGRFDPKTGT 220
|
250 260 270
....*....|....*....|....*....|....*..
gi 917733955 475 FQaHFVNEYLEDGPQeqmilSLTTANNG-IWVGTTNG 510
Cdd:COG4257 221 VT-EYPLPGGGARPY-----GVAVDGDGrVWFAESGA 251
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
925-1051 |
8.08e-06 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 50.15 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 925 EEALRLSSQVLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFlfltRGLYDRSFYQQIehqLLNQKHWSGEV 1004
Cdd:COG3829 7 KELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNV----TELIPNSPLLEV---LKTGKPVTGVI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 917733955 1005 QIRTHCKQPLLVwmeVNQVLNSQGEASHFVVVFTDITDRKQAEEDLR 1051
Cdd:COG3829 80 QKTGGKGKTVIV---TAIPIFEDGEVIGAVETFRDITELKRLERKLR 123
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
935-1045 |
1.48e-05 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 45.48 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 935 LESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFlfltRGLYDRSFYQQIEHQLlnQKHWSGEVQIRTHCKQPL 1014
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTL----AELLPPEDAARLERAL--RRALEGEEPIDFLEELLL 74
|
90 100 110
....*....|....*....|....*....|....*.
gi 917733955 1015 ---LVWMEVNQ--VLNSQGEASHFVVVFTDITDRKQ 1045
Cdd:pfam08448 75 ngeERHYELRLtpLRDPDGEVIGVLVISRDITERRR 110
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
841-1055 |
3.89e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 48.52 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 841 APAETNASRQMA--LVHPDDRPQVQAA-------LESYLQGDtEFFEAEYRIKLTDANWSWVLDRgkiVERDRSGKpLRL 911
Cdd:PRK13560 108 AKHDLMADKGLLamLIGGDDGDFFFANpfrsaetIAMALQSD-DWQEEEGHFRCGDGRFIDCCLR---FERHAHAD-DQV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 912 AGTFTDISMRRGQE----EALRLSSQVLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFLFLTRGlYDRSFY 987
Cdd:PRK13560 183 DGFAEDITERKRAEeridEALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPA-QPADDY 261
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 917733955 988 QQIEHQLLN---QKHWSGEVQIRTHCKQPLLVWMEVNQVLNSQGEASHFVVVFTDITDRKQAEEDLRLLAN 1055
Cdd:PRK13560 262 QEADAAKFDadgSQIIEAEFQNKDGRTRPVDVIFNHAEFDDKENHCAGLVGAITDISGRRAAERELLEKED 332
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
932-994 |
6.94e-05 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 42.39 E-value: 6.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 917733955 932 SQVLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFLFLTRGLYDRSFYQQIEHQL 994
Cdd:smart00091 4 RAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLL 66
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
1327-1466 |
9.16e-05 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 45.76 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 1327 QSDIISSIEV------ALAMHGLAADLLE------IELTESAVMqqPLESveILNQLKGLGlSLAVDDFGTG---YSSLA 1391
Cdd:PRK11596 97 RHGLLASVNIdgptliALRQQPAILRLIErlpwlrFELVEHIRL--PKDS--PFASMCEFG-PLWLDDFGTGmanFSALS 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917733955 1392 YLKrfpLDTLKIDREFVRDITKDPDDAAITSAIIVLAHSLELQVVAEGVETQAQLNFLAAQGCDQAQGFLLGRPM 1466
Cdd:PRK11596 172 EVR---YDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPA 243
|
|
| Reg_prop |
pfam07494 |
Two component regulator propeller; A large group of two component regulator proteins appear to ... |
38-61 |
6.25e-04 |
|
Two component regulator propeller; A large group of two component regulator proteins appear to have the same N-terminal structure of 14 tandem repeats. These repeats show homology to pfam01011 and pfam00400 indicating that they are likely to form a beta-propeller. This family has been built with artificially high cut-offs in order to avoid overlaps with other beta-propeller families. The fourteen repeats are likely to form two propellers; it is not clear if these structures are likely to recruit other proteins or interact with DNA.
Pssm-ID: 400050 [Multi-domain] Cd Length: 24 Bit Score: 38.45 E-value: 6.25e-04
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
933-975 |
8.60e-04 |
|
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 39.07 E-value: 8.60e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 917733955 933 QVLESMNESVVVCDLNYRIISVNPAFCSTTGFSEQQIACKPFL 975
Cdd:pfam13188 5 ALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELL 47
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
911-1052 |
8.75e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 43.89 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 911 LAGTFTDISMRRGQEEALRLSS----QVLESMNESVVVCDLNYRIISV-NPAFCSTTGFSEQQIACKPFLF----LTRGL 981
Cdd:PRK13560 310 LVGAITDISGRRAAERELLEKEdmlrAIIEAAPIAAIGLDADGNICFVnNNAAERMLGWSAAEVMGKPLPGmdpeLNEEF 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917733955 982 YDRSFYQ-------------QIEHQLLNQKHWSGeVQIRTHCKQ--PLLVWMEVNQVLNSQGEASHFVVVFTDITDRKQA 1046
Cdd:PRK13560 390 WCGDFQEwypdgrpmafdacPMAKTIKGGKIFDG-QEVLIEREDdgPADCSAYAEPLHDADGNIIGAIALLVDITERKQV 468
|
....*.
gi 917733955 1047 EEDLRL 1052
Cdd:PRK13560 469 EEQLLL 474
|
|
| Reg_prop |
pfam07494 |
Two component regulator propeller; A large group of two component regulator proteins appear to ... |
83-106 |
9.82e-04 |
|
Two component regulator propeller; A large group of two component regulator proteins appear to have the same N-terminal structure of 14 tandem repeats. These repeats show homology to pfam01011 and pfam00400 indicating that they are likely to form a beta-propeller. This family has been built with artificially high cut-offs in order to avoid overlaps with other beta-propeller families. The fourteen repeats are likely to form two propellers; it is not clear if these structures are likely to recruit other proteins or interact with DNA.
Pssm-ID: 400050 [Multi-domain] Cd Length: 24 Bit Score: 37.68 E-value: 9.82e-04
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
853-928 |
1.12e-03 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 40.35 E-value: 1.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917733955 853 LVHPDDRPQVQAALESYLQGDTEFFEAEYRIKLTDANWSWVLDRGKIVERDrsGKPLRLAGTFTDISMRRGQEEAL 928
Cdd:TIGR00229 51 LIPEEDREEVRERIERRLEGEPEPVSEERRVRRKDGSEIWVEVSVSPIRTN--GGELGVVGIVRDITERKEAEEAL 124
|
|
| Reg_prop |
pfam07494 |
Two component regulator propeller; A large group of two component regulator proteins appear to ... |
301-322 |
1.48e-03 |
|
Two component regulator propeller; A large group of two component regulator proteins appear to have the same N-terminal structure of 14 tandem repeats. These repeats show homology to pfam01011 and pfam00400 indicating that they are likely to form a beta-propeller. This family has been built with artificially high cut-offs in order to avoid overlaps with other beta-propeller families. The fourteen repeats are likely to form two propellers; it is not clear if these structures are likely to recruit other proteins or interact with DNA.
Pssm-ID: 400050 [Multi-domain] Cd Length: 24 Bit Score: 37.29 E-value: 1.48e-03
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
853-918 |
2.55e-03 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 38.77 E-value: 2.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 917733955 853 LVHPDDRPQVQAALESYLQGDtEFFEAEYRIKLTDANWSWVLDRGKIVeRDRSGKPLRLAGTFTDI 918
Cdd:cd00130 40 LIHPEDREELRERLENLLSGG-EPVTLEVRLRRKDGSVIWVLVSLTPI-RDEGGEVIGLLGVVRDI 103
|
|
| |
